Potassium in PDB 3syq: Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2

The structure of Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2, PDB code: 3syq was solved by M.R.Whorton, R.Mackinnon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.39 / 3.44
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	87.605, 208.491, 117.376, 90.00, 90.00, 90.00
R / Rfree (%)	29.9 / 32.3

The binding sites of Potassium atom in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2 (pdb code 3syq). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2, PDB code: 3syq:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2 within 5.0Å range: probe atom residue distance (Å) B Occ A:K501 b:0.1 occ:0.25 K A:K502 2.8 1.0 0.3 O A:GLY156 3.0 0.2 1.0 O B:GLY156 3.1 0.8 1.0 O B:TYR157 3.2 0.5 1.0 O A:TYR157 3.5 0.6 1.0 C B:TYR157 3.6 0.8 1.0 C A:TYR157 3.7 0.5 1.0 CA A:TYR157 4.1 0.4 1.0 CA B:TYR157 4.1 0.9 1.0 C A:GLY156 4.1 0.1 1.0 C B:GLY156 4.2 0.6 1.0 N B:GLY158 4.2 0.7 1.0 N A:GLY158 4.4 0.8 1.0 CA B:GLY158 4.6 0.4 1.0 N A:TYR157 4.6 0.9 1.0 N B:TYR157 4.6 0.4 1.0 CA A:GLY158 4.9 0.7 1.0 O A:ILE155 4.9 0.7 1.0

Potassium binding site 2 out of 4 in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2 within 5.0Å range: probe atom residue distance (Å) B Occ A:K502 b:1.0 occ:0.25 O A:ILE155 2.7 0.7 1.0 O B:GLY156 2.8 0.8 1.0 K A:K501 2.8 0.1 0.3 O A:GLY156 2.9 0.2 1.0 O B:ILE155 3.0 0.3 1.0 K A:K503 3.1 96.2 0.2 C B:GLY156 3.8 0.6 1.0 C A:GLY156 3.9 0.1 1.0 C A:ILE155 4.0 0.9 1.0 C B:ILE155 4.2 0.6 1.0 CA A:GLY156 4.5 1.0 1.0 CA B:GLY156 4.6 0.4 1.0 N A:GLY156 4.7 0.8 1.0 N B:TYR157 4.7 0.4 1.0 N A:TYR157 4.8 0.9 1.0 N B:GLY156 4.9 0.6 1.0 CA B:TYR157 4.9 0.9 1.0 CA A:ILE155 5.0 0.9 1.0 CA A:TYR157 5.0 0.4 1.0

Potassium binding site 3 out of 4 in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2 within 5.0Å range: probe atom residue distance (Å) B Occ A:K503 b:96.2 occ:0.25 O B:ILE155 2.8 0.3 1.0 O A:THR154 2.8 0.8 1.0 O A:ILE155 2.8 0.7 1.0 K A:K502 3.1 1.0 0.3 O B:THR154 3.1 0.6 1.0 K A:K504 3.3 0.7 0.3 C A:ILE155 3.7 0.9 1.0 C B:ILE155 3.7 0.6 1.0 CA A:ILE155 3.8 0.9 1.0 C A:THR154 3.9 0.8 1.0 CA B:ILE155 4.0 0.7 1.0 C B:THR154 4.2 0.4 1.0 N A:ILE155 4.4 0.5 1.0 N B:ILE155 4.6 0.2 1.0 N A:GLY156 4.9 0.8 1.0 N B:GLY156 4.9 0.6 1.0 O B:GLY156 4.9 0.8 1.0

Potassium binding site 4 out of 4 in the Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Crystal Structure of the G Protein-Gated Inward Rectifier K+ Channel GIRK2 (KIR3.2) R201A Mutant in Complex with PIP2 within 5.0Å range: probe atom residue distance (Å) B Occ A:K504 b:0.7 occ:0.25 OG1 A:THR154 2.7 0.1 1.0 O B:THR154 2.8 0.6 1.0 O A:THR154 2.9 0.8 1.0 OG1 B:THR154 3.0 0.9 1.0 K A:K503 3.3 96.2 0.2 CB A:THR154 3.8 0.2 1.0 C A:THR154 3.8 0.8 1.0 C B:THR154 3.9 0.4 1.0 CB B:THR154 4.0 0.5 1.0 O A:THR153 4.4 0.7 1.0 CA A:THR154 4.4 0.8 1.0 CA B:THR154 4.6 0.4 1.0 N A:ILE155 4.7 0.5 1.0 O B:THR153 4.8 0.2 1.0 N B:ILE155 4.8 0.2 1.0 CA B:ILE155 5.0 0.7 1.0

M.R.Whorton, R.Mackinnon. Crystal Structure of the Mammalian GIRK2 K(+) Channel and Gating Regulation By G Proteins, Pip(2), and Sodium. Cell(Cambridge,Mass.) V. 147 199 2011.
ISSN: ISSN 0092-8674
PubMed: 21962516
DOI: 10.1016/J.CELL.2011.07.046